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Nei endonuclease VIII-like 1

NEIL1, endonuclease VIII, Nei-like
This gene is a member of the Nei endonuclease VIII-like gene family which encodes DNA glycosylases. The encoded enzyme participates in the DNA repair pathway by initiating base excision repair by removing damaged bases, primarily oxidized pyrimidines. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Feb 2012] (from NCBI)
Top mentioned proteins: NEI, OGG1, NEIL2, NTH1, CAN
Papers on NEIL1
Neil DNA glycosylases promote substrate turnover by Tdg during DNA demethylation.
Niehrs et al., Mainz, Germany. In Nat Struct Mol Biol, Feb 2016
Here we show that human NEIL1 and NEIL2 DNA glycosylases coordinate abasic-site processing during TET-TDG DNA demethylation.
Base and Nucleotide Excision Repair of Oxidatively Generated Guanine Lesions in DNA.
Geacintov et al., New York City, United States. In J Biol Chem, Feb 2016
In the case of mouse embryonic fibroblasts, BER of the Sp lesion is strongly reduced in NEIL1(-/-) relative to NEIL1(+/+) extracts.
3CAPS - a structural AP-site analogue as a tool to investigate DNA base excision repair.
Schär et al., Bern, Switzerland. In Nucleic Acids Res, Feb 2016
The AP lyase activity of bifunctional DNA glycosylases (NTH1, NEIL1, FPG), however, was fully inhibited.
Whole exome sequencing identifies rare protein-coding variants in Behçet's disease.
Sawalha et al., Ann Arbor, United States. In Arthritis Rheumatol, Jan 2016
We detected genetic association between BD and LIMK2 (rs149034313), involved in regulating cytoskeletal reorganization, and NEIL1 (rs5745908), involved in base excision DNA repair (P=3.22x10(-4) and P=5.16x10(-4) , respectively).
Gene amplification-associated overexpression of the RNA editing enzyme ADAR1 enhances human lung tumorigenesis.
Esteller et al., Barcelona, Spain. In Oncogene, Jan 2016
From a functional perspective, ADAR1 overexpression enhances the editing frequencies of target transcripts such as NEIL1 and miR-381.
Neil2-null Mice Accumulate Oxidized DNA Bases in the Transcriptionally Active Sequences of the Genome and Are Susceptible to Innate Inflammation.
Hazra et al., Berkeley, United States. In J Biol Chem, Nov 2015
Here, we report the generation and characterization of mice lacking Neil2 (Nei-like 2).
Guanine oxidation product 5-carboxamido-5-formamido-2-iminohydantoin induces mutations when bypassed by DNA polymerases and is a substrate for base excision repair.
Burrows et al., Salt Lake City, United States. In Chem Res Toxicol, Oct 2015
Both diastereomer lesions were found to be substrates for the DNA glycosylases NEIL1 and Fpg, and poorly excised by endonuclease III (Nth).
A Role for the Fifth G-Track in G-Quadruplex Forming Oncogene Promoter Sequences during Oxidative Stress: Do These "Spare Tires" Have an Evolved Function?
Burrows et al., Salt Lake City, United States. In Acs Cent Sci, Sep 2015
These new "spare tire"-containing strands with Gh in loops are now found to be substrates for initiation of BER with the NEIL1, NEIL2, and NEIL3 DNA glycosylases.
The C-terminal Domain (CTD) of Human DNA Glycosylase NEIL1 Is Required for Forming BERosome Repair Complex with DNA Replication Proteins at the Replicating Genome: DOMINANT NEGATIVE FUNCTION OF THE CTD.
Hegde et al., Houston, United States. In J Biol Chem, Sep 2015
The human DNA glycosylase NEIL1 was recently demonstrated to initiate prereplicative base excision repair (BER) of oxidized bases in the replicating genome, thus preventing mutagenic replication.
New paradigms in the repair of oxidative damage in human genome: mechanisms ensuring repair of mutagenic base lesions during replication and involvement of accessory proteins.
Hegde et al., Houston, United States. In Cell Mol Life Sci, May 2015
Following up our earlier studies, which showed that the Nei endonuclease VIII like 1 (NEIL1) DNA glycosylase, one of the five base excision repair (BER)-initiating enzymes in mammalian cells, has enhanced expression during the S-phase and higher affinity for replication fork-mimicking single-stranded (ss) DNA substrates, we recently provided direct experimental evidence for NEIL1's role in replicating template strand repair.
Variation in DNA Base Excision Repair Genes in Fuchs Endothelial Corneal Dystrophy.
Szaflik et al., Łódź, Poland. In Med Sci Monit, 2014
In this work, we searched for the association between variation of the PARP-1, NEIL1, POLG, and XRCC1 genes and FECD occurrence.
DNA glycosylases search for and remove oxidized DNA bases.
Wallace, Burlington, United States. In Environ Mol Mutagen, 2013
For example, even though human NEIL1 and the plant and fungal orthologs lack the zinc finger shown to be required for binding, DNA crystal structures revealed a "zincless finger" with the same properties.
NEIL1 binding to DNA containing 2'-fluorothymidine glycol stereoisomers and the effect of editing.
Beal et al., Davis, United States. In Chembiochem, 2012
the binding of these modified DNAs with the unedited and edited forms of human NEIL1 along with E. coli Endo III
Structural characterization of viral ortholog of human DNA glycosylase NEIL1 bound to thymine glycol or 5-hydroxyuracil-containing DNA.
Doublié et al., Burlington, United States. In J Biol Chem, 2012
Structural characterization of viral ortholog of human DNA glycosylase NEIL1 bound to thymine glycol or 5-hydroxyuracil-containing DNA.
NEIL1 mRNA splicing variants are expressed in normal mouse organs.
Kubo et al., Ōsaka, Japan. In J Radiat Res (tokyo), 2011
These results suggest that mNEIL1 mRNA variants are expressed in a variety of organs in normal mice and that variant 1 protein may regulate mNEIL1 activity.
The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage.
Wallace et al., Burlington, United States. In Prog Mol Biol Transl Sci, 2011
The bifunctional formamidopyrimidine DNA glycosylase (Fpg) and endonuclease VIII (Nei) are members of the Fpg/Nei family, one of the two families of glycosylases that recognize oxidized DNA bases, the other being the HhH/GPD (or Nth) superfamily.
Exome sequencing identified MYO1E and NEIL1 as candidate genes for human autosomal recessive steroid-resistant nephrotic syndrome.
Gharavi et al., New York City, United States. In Kidney Int, 2011
Homozygosity mapping and exome sequencing in a consanguineous kindred identified MYO1E and NEIL1 as novel candidate genes for human autosomal recessive steroid-resistant nephrotic syndrome.
Variable penetrance of metabolic phenotypes and development of high-fat diet-induced adiposity in NEIL1-deficient mice.
R Stephen et al., Portland, United States. In Am J Physiol Endocrinol Metab, 2011
NEIL1 deficiency results in an increased susceptibility to obesity and related complications potentially by lowering the threshold for tolerance of cellular oxidative stress in neil1(-/-) mice.
Eukaryotic endonuclease VIII-like proteins: new components of the base excision DNA repair system.
Zharkov et al., Novosibirsk, Russia. In Biochemistry (mosc), 2011
In 2002, three new human DNA glycosylases (NEIL1, NEIL2, and NEIL3) were discovered, all homologous to endonuclease VIII, a bacterial protein, which also participates in DNA repair.
The Fanconi anemia pathway promotes DNA glycosylase-dependent excision of interstrand DNA crosslinks.
Saparbaev et al., Villejuif, France. In Environ Mol Mutagen, 2010
Recently, we reported that human oxidative DNA glycosylase, NEIL1 excises with high efficiency the unhooked crosslinked oligomer within three-stranded DNA repair intermediate induced by photoactivated psoralen exposure.
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